PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
30810528-2	2019	Previous studies in yeast revealed that the autophagy-related E3 complex Atg12-Atg5-Atg16 is recruited to the PAS via Atg16 interaction with Atg21, which binds phosphatidylinositol 3-phosphate (PI3P) produced at the PAS, to stimulate conjugation of the ubiquitin-like protein Atg8 to phosphatidylethanolamine.	Aminosalicylic Acid	110-113	Atg21p	Saccharomyces cerevisiae S288C	141-146	
30810528-2	2019	Previous studies in yeast revealed that the autophagy-related E3 complex Atg12-Atg5-Atg16 is recruited to the PAS via Atg16 interaction with Atg21, which binds phosphatidylinositol 3-phosphate (PI3P) produced at the PAS, to stimulate conjugation of the ubiquitin-like protein Atg8 to phosphatidylethanolamine.	Aminosalicylic Acid	216-219	Atg21p	Saccharomyces cerevisiae S288C	141-146	
27560294-2	2016	Atg21 binds via 2 sites at the circumference of its beta-propeller to PtdIns3P at the phagophore assembly site (PAS).	Aminosalicylic Acid	112-115	Atg21p	Saccharomyces cerevisiae S288C	0-5